LST7_YEAST
ID LST7_YEAST Reviewed; 242 AA.
AC P53237; D6VUJ2; Q45U29;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein LST7;
DE AltName: Full=Lethal with SEC thirteen protein 7;
GN Name=LST7; OrderedLocusNames=YGR057C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=9409822; DOI=10.1093/genetics/147.4.1569;
RA Roberg K.J., Bickel S., Rowley N., Kaiser C.A.;
RT "Control of amino acid permease sorting in the late secretory pathway of
RT Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8.";
RL Genetics 147:1569-1584(1997).
RN [5]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=32801125; DOI=10.1242/jcs.245555;
RA Uemura S., Mochizuki T., Amemiya K., Kurosaka G., Yazawa M., Nakamoto K.,
RA Ishikawa Y., Izawa S., Abe F.;
RT "Amino acid homeostatic control by TORC1 in Saccharomyces cerevisiae under
RT high hydrostatic pressure.";
RL J. Cell Sci. 133:jcs245555-jcs245555(2020).
CC -!- FUNCTION: Required for the nitrogen-regulated transport of amino acid
CC permeases GAP1 and PUT4 from the Golgi to the cell surface.
CC {ECO:0000269|PubMed:9409822}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to high hydrostatic pressure
CC (mechanical stress). {ECO:0000269|PubMed:32801125}.
CC -!- MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA97058.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA97060.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ115391; AAZ22470.1; -; Genomic_DNA.
DR EMBL; Z72842; CAA97058.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z72843; CAA97060.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006941; DAA08153.1; -; Genomic_DNA.
DR PIR; S64351; S64351.
DR RefSeq; NP_011571.4; NM_001181186.3.
DR AlphaFoldDB; P53237; -.
DR SMR; P53237; -.
DR BioGRID; 33302; 161.
DR DIP; DIP-1424N; -.
DR IntAct; P53237; 2.
DR MINT; P53237; -.
DR STRING; 4932.YGR057C; -.
DR MaxQB; P53237; -.
DR PaxDb; P53237; -.
DR PRIDE; P53237; -.
DR EnsemblFungi; YGR057C_mRNA; YGR057C; YGR057C.
DR GeneID; 852948; -.
DR KEGG; sce:YGR057C; -.
DR SGD; S000003289; LST7.
DR VEuPathDB; FungiDB:YGR057C; -.
DR eggNOG; KOG3715; Eukaryota.
DR GeneTree; ENSGT00390000009864; -.
DR HOGENOM; CLU_035854_1_0_1; -.
DR InParanoid; P53237; -.
DR OMA; THFCDKH; -.
DR BioCyc; YEAST:G3O-30774-MON; -.
DR PRO; PR:P53237; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53237; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:1990877; C:FNIP-folliculin RagC/D GAP; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IMP:SGD.
DR InterPro; IPR037521; FLCN/SMCR8_DENN.
DR InterPro; IPR021713; Folliculin.
DR InterPro; IPR037520; Folliculin/SMCR8_longin.
DR PANTHER; PTHR31441; PTHR31441; 1.
DR Pfam; PF11704; Folliculin; 1.
DR PROSITE; PS51834; DENN_FLCN_SMCR8; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..242
FT /note="Protein LST7"
FT /id="PRO_0000202801"
FT DOMAIN 48..212
FT /note="uDENN FLCN/SMCR8-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01178"
FT VARIANT 4
FT /note="T -> I (in strain: SK1)"
SQ SEQUENCE 242 AA; 28136 MW; 410B0A6E670FACA2 CRC64;
MSSTVISLAH FCDKHGPRII SVTQSAEKGT LGEELLVPDY PTESYCESCL LQFPEESTRS
MRCFIEDVPF ITTQYSSIRY QLLNSIIKRA FSEETMIYDN MPFIFFDDLR GLNLVIGFKL
YDENARGNER RYCFILTVDS RSHDDSMKML SEHWNFIIGG FDKMIAYIKN IHKSEFLGKN
KTVENNLETL NNNAFIGSYL RANKSKFGRN LVSLTDDKFL FVRIHKWNSF LLHTVMNENK
LP
